P31040 (DHSA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
EC=1.3.5.1

Alternative name(s):
Flavoprotein subunit of complex II
Short name=Fp

Gene names

Name:	SDHA
Synonyms:	SDH2, SDHF

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	664 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor. Ref.12
Catalytic activity	Succinate + ubiquinone = fumarate + ubiquinol.
Cofactor	FAD.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.
Subunit structure	Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD. Interacts with SDHAF2/SDH5; interaction is required for FAD attachment. Ref.10
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Involvement in disease	Mitochondrial complex II deficiency (MT-C2D) [MIM:252011]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations. Clinical features include psychomotor regression in infants, poor growth with lack of speech development, severe spastic quadriplegia, dystonia, progressive leukoencephalopathy, muscle weakness, exercise intolerance, cardiomyopathy. Some patients manifest Leigh syndrome or Kearns-Sayre syndrome. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.8 Cardiomyopathy, dilated 1GG (CMD1GG) [MIM:613642]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Paragangliomas 5 (PGL5) [MIM:614165]: A neural crest tumor usually derived from the chromoreceptor tissue of a paraganglion. Paragangliomas can develop at various body sites, including the head, neck, thorax and abdomen. Most commonly, they are located in the head and neck region, specifically at the carotid bifurcation, the jugular foramen, the vagal nerve, and in the middle ear. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12
Miscellaneous	The complex, present in mitochondria, can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone.
Sequence similarities	Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
Sequence caution	The sequence CAA37886.1 differs from that shown. Reason: Differs extensively from that shown.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Disease	Cardiomyopathy Disease mutation Leigh syndrome Tumor suppressor
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	nervous system development Inferred from mutant phenotype PubMed 16361598. Source: UniProtKB respiratory electron transport chain Inferred from direct assay Ref.8. Source: UniProtKB succinate metabolic process Inferred from direct assay Ref.8. Source: UniProtKB tricarboxylic acid cycle Traceable author statement Ref.8. Source: UniProtKB
Cellular_component	mitochondrial respiratory chain complex II Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro succinate dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SDHB	P21912	2	EBI-1057265,EBI-1056481

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 43	43	Mitochondrion By similarity
	Chain	44 – 664	621	Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial		PRO_0000010335
Regions
	Nucleotide binding	68 – 73	6	FAD By similarity
	Nucleotide binding	91 – 106	16	FAD By similarity
	Nucleotide binding	456 – 457	2	FAD By similarity
Sites
	Active site	340	1	Proton acceptor By similarity
	Binding site	275	1	FAD By similarity
	Binding site	296	1	Substrate By similarity
	Binding site	308	1	Substrate By similarity
	Binding site	407	1	Substrate By similarity
	Binding site	440	1	FAD By similarity
	Binding site	451	1	Substrate By similarity
Amino acid modifications
	Modified residue	99	1	Tele-8alpha-FAD histidine By similarity
	Modified residue	179	1	N6-acetyllysine Ref.11
	Modified residue	252	1	Phosphothreonine By similarity
	Modified residue	335	1	N6-acetyllysine Ref.11
	Modified residue	485	1	N6-acetyllysine By similarity
	Modified residue	498	1	N6-acetyllysine By similarity
	Modified residue	538	1	N6-acetyllysine By similarity
	Modified residue	541	1	N6-acetyllysine Ref.11
	Modified residue	547	1	N6-acetyllysine By similarity
	Modified residue	608	1	N6-acetyllysine Ref.11
Natural variations
	Natural variant	33	1	F → V. Corresponds to variant rs1061518 [ dbSNP | Ensembl ].		VAR_049214
	Natural variant	38	1	D → V. Corresponds to variant rs34635677 [ dbSNP | Ensembl ].		VAR_049215
	Natural variant	240	1	E → Q. Corresponds to variant rs1041946 [ dbSNP | Ensembl ].		VAR_049216
	Natural variant	333	1	V → I. Corresponds to variant rs1062468 [ dbSNP | Ensembl ].		VAR_059307
	Natural variant	524	1	A → V in LS. Ref.3		VAR_016878
	Natural variant	554	1	R → W in LS. Ref.8		VAR_002449
	Natural variant	555	1	G → E in MT-C2D and CMD1GG. Ref.14 Ref.15		VAR_016879
	Natural variant	589	1	R → W in PGL5; loss of activity. Ref.12		VAR_065975
	Natural variant	657	1	V → I. Ref.2 Corresponds to variant rs6962 [ dbSNP | Ensembl ].		VAR_049217
Experimental info
	Sequence conflict	356	1	G → D in AAD51006. Ref.3
	Sequence conflict	398	1	E → D in AAD51006. Ref.3
	Sequence conflict	591	1	A → T in AAD51006. Ref.3
	Sequence conflict	596	1	D → G in AAD51006. Ref.3
	Sequence conflict	600	1	R → Q in AAD51006. Ref.3
	Sequence conflict	629	1	Y → F in AAA20683. Ref.2
	Sequence conflict	640	1	E → G in AAD51006. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P31040 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 180B664E3FFD0B34	FASTA	664	72,692
	10 20 30 40 50 60 MSGVRGLSRL LSARRLALAK AWPTVLQTGT RGFHFTVDGN KRASAKVSDS ISAQYPVVDH 70 80 90 100 110 120 EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT VAAQGGINAA LGNMEEDNWR 130 140 150 160 170 180 WHFYDTVKGS DWLGDQDAIH YMTEQAPAAV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF 190 200 210 220 230 240 GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE 250 260 270 280 290 300 DGSIHRIRAK NTVVATGGYG RTYFSCTSAH TSTGDGTAMI TRAGLPCQDL EFVQFHPTGI 310 320 330 340 350 360 YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE 370 380 390 400 410 420 KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ 430 440 450 460 470 480 VLRHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IEESCRPGDK 490 500 510 520 530 540 VPPIKPNAGE ESVMNLDKLR FADGSIRTSE LRLSMQKSMQ NHAAVFRVGS VLQEGCGKIS 550 560 570 580 590 600 KLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR 610 620 630 640 650 660 IDEYDYSKPI QGQQKKPFEE HWRKHTLSYV DVGTGKVTLE YRPVIDKTLN EADCATVPPA IRSY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the flavoprotein (Fp) subunit of liver mitochondria." Hirawake H., Wang H., Kuramochi T., Kojima S., Kita K. J. Biochem. 116:221-227(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"The cDNA sequence of the flavoprotein subunit of human heart succinate dehydrogenase." Morris A.A.M., Farnsworth L., Ackrell B.A.C., Turnbull D.M., Birch-MacHin M.A. Biochim. Biophys. Acta 1185:125-128(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-657. Tissue: Heart.
[3]	"Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome." Parfait B., Chretien D., Roetig A., Marsac C., Munnich A., Rustin P. Hum. Genet. 106:236-243(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LS VAL-524.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[7]	"Cloning of the flavoprotein subunit of human succinate dehydrogenase." Malcovati M., Marchetti L., Zanelli E., Tenchini M.L. (In) Curti B., Ronchi S., Zanetti G. (eds.); Flavins and flavoproteins 1990, pp.727-730, Walter de Gruyter, Berlin (1991) Cited for: PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[8]	"Mutation of a nuclear succinate dehydrogenase gene results in mitochondrial respiratory chain deficiency." Bourgeron T., Rustin P., Chretien D., Birch-MacHin M.A., Bourgeois M., Viegas-Pequignot E., Munnich A., Roetig A. Nat. Genet. 11:144-149(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 546-562, VARIANT LS TRP-554.
[9]	"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V. Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 76-92 AND 398-418. Tissue: Adipocyte.
[10]	"SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma." Hao H.-X., Khalimonchuk O., Schraders M., Dephoure N., Bayley J.-P., Kunst H., Devilee P., Cremers C.W.R.J., Schiffman J.D., Bentz B.G., Gygi S.P., Winge D.R., Kremer H., Rutter J. Science 325:1139-1142(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SDHAF2.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-335; LYS-541 AND LYS-608, MASS SPECTROMETRY.
[12]	"SDHA is a tumor suppressor gene causing paraganglioma." Burnichon N., Briere J.J., Libe R., Vescovo L., Riviere J., Tissier F., Jouanno E., Jeunemaitre X., Benit P., Tzagoloff A., Rustin P., Bertherat J., Favier J., Gimenez-Roqueplo A.P. Hum. Mol. Genet. 19:3011-3020(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, VARIANT PGL5 TRP-589, CHARACTERIZATION OF VARIANT PGL5 TRP-589.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II." Van Coster R., Seneca S., Smet J., Van Hecke R., Gerlo E., Devreese B., Van Beeumen J., Leroy J.G., De Meirleir L., Lissens W. Am. J. Med. Genet. A 120:13-18(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MT-C2D GLU-555.
[15]	"Familial neonatal isolated cardiomyopathy caused by a mutation in the flavoprotein subunit of succinate dehydrogenase." Levitas A., Muhammad E., Harel G., Saada A., Caspi V.C., Manor E., Beck J.C., Sheffield V., Parvari R. Eur. J. Hum. Genet. 18:1160-1165(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMD1GG GLU-555.
+	Additional computationally mapped references.

Web resources

TCA Cycle Gene Mutation Database

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	D30648 mRNA. Translation: BAA06332.1. L21936 mRNA. Translation: AAA20683.1. AF171030 , AF171017, AF171018, AF171019, AF171020, AF171021, AF171022, AF171023, AF171024, AF171025, AF171026, AF171027, AF171028, AF171029 Genomic DNA. Translation: AAD51006.1. AK291311 mRNA. Translation: BAF84000.1. CH471235 Genomic DNA. Translation: EAW50983.1. BC001380 mRNA. Translation: AAH01380.1. X53943 mRNA. Translation: CAA37886.1. Sequence problems. S79641 Genomic DNA. Translation: AAB35332.1.
IPI	IPI00305166.
PIR	JX0336. S21302.
RefSeq	NP_004159.2. NM_004168.2.
UniGene	Hs.440475.
3D structure databases
ProteinModelPortal	P31040.
ModBase	Search...
Protein-protein interaction databases
IntAct	P31040. 14 interactions.
STRING	9606.ENSP00000264932.
PTM databases
PhosphoSite	P31040.
Polymorphism databases
DMDM	1169337.
2D gel databases
REPRODUCTION-2DPAGE	IPI00305166.
Proteomic databases
PaxDb	P31040.
PeptideAtlas	P31040.
PRIDE	P31040.
Protocols and materials databases
DNASU	6389.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264932; ENSP00000264932; ENSG00000073578.
GeneID	6389.
KEGG	hsa:6389.
UCSC	uc003jao.4. human.
Organism-specific databases
CTD	6389.
GeneCards	GC05P000208.
H-InvDB	HIX0120996.
HGNC	HGNC:10680. SDHA.
HPA	CAB034929.
MIM	252011. phenotype. 256000. phenotype. 600857. gene. 613642. phenotype. 614165. phenotype.
neXtProt	NX_P31040.
Orphanet	154. Familial isolated dilated cardiomyopathy. 29072. Hereditary pheochromocytoma-paraganglioma. 3208. Isolated succinate-CoQ reductase deficiency. 255241. Leigh syndrome with leukodystrophy.
PharmGKB	PA35605.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1053.
HOVERGEN	HBG001461.
InParanoid	P31040.
KO	K00234.
OMA	CFTADAT.
OrthoDB	EOG47H5PJ.
PhylomeDB	P31040.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000073578-MONOMER.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00223; UER01006.
Gene expression databases
ArrayExpress	P31040.
Bgee	P31040.
CleanEx	HS_SDHA.
Genevestigator	P31040.
GermOnline	ENSG00000073578. Homo sapiens.
Family and domain databases
Gene3D	1.20.58.100. 1 hit.
InterPro	IPR003953. FAD_bind_dom. IPR003952. FRD_SDH_FAD_BS. IPR015939. Fum_Rdtase/Succ_DH_flav-like_C. IPR011281. Succ_DH_flav_su_fwd. IPR014006. Succ_Dhase_FrdA_Gneg. [Graphical view]
PANTHER	PTHR11632:SF5. PTHR11632:SF5. 1 hit.
Pfam	PF00890. FAD_binding_2. 1 hit. PF02910. Succ_DH_flav_C. 1 hit. [Graphical view]
SUPFAM	SSF46977. Succ_DH_flav_C. 1 hit.
TIGRFAMs	TIGR01816. sdhA_forward. 1 hit. TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITE	PS00504. FRD_SDH_FAD_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL5758.
DrugBank	DB00139. Succinic acid.
GenomeRNAi	6389.
NextBio	24820.
SOURCE	Search...

Entry information

Entry name

DHSA_HUMAN

Accession

Primary (citable) accession number: P31040
Secondary accession number(s): A8K5J6, Q16395, Q9UMY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 154 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.